ID   R4XGU5_TAPDE            Unreviewed;       497 AA.
AC   R4XGU5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   SubName: Full=Putatitve vacuolar aspartyl aminopeptidase Lap4 {ECO:0000313|EMBL:CCG84907.1};
GN   ORFNames=TAPDE_005470 {ECO:0000313|EMBL:CCG84907.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG84907.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG84907.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCG84907.1}.
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DR   EMBL; CAHR02000343; CCG84907.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4XGU5; -.
DR   STRING; 1097556.R4XGU5; -.
DR   VEuPathDB; FungiDB:TAPDE_005470; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   Proteomes; UP000013776; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF4; VACUOLAR AMINOPEPTIDASE 1; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  53917 MW;  55737EF3C0E6E97D CRC64;
     MQIQVTTSHH DQTRAPSRAS SAVFKETDKH GQGFCDFLNA TPTVFHAVDF YSTRLKASGY
     KHLAERDDWS ETLKAGGKYF FTRNYSSLIA FTIGEKYVAG NGIAIIGSHI DALTMRVKPV
     STKSSAGYLQ LAVAPYAGGG NMTWWDRDLG LAGRVMVSDA SGGIKQHLVR LPYPIAKIPT
     LAPHFGAPSR GPFDAETQMT PIVGLEPQTV EHELEKQFNV LSTDAVNNPQ KNHSPRLLAA
     VAKQLGIKVS QISDFELELF DFQPAQPFGL DGELLSVPRC DDKLCSYAAM EALLNCTSDR
     ECITQSGAIH MVYLCDDEEV GSGLRQGAGG NMVPLAVERI VDVLNKSDKR TQNLVAMTFA
     RSFLISADVK HALNPNFVGA YEPNMAPRLN VGPVISCDAN AHMTTDAVSK SFCQKIANRA
     GSTLQLFQIR NGQPSGGTIG PMLSSKTGIR AIDIGIPQLA MHSIRATTGA KDPGLGVKYF
     EAFFRQFEEV EGTIKVD
//